ID A0A430BNJ7_9SPHN Unreviewed; 380 AA.
AC A0A430BNJ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=RIP metalloprotease RseP {ECO:0000313|EMBL:RSU54305.1};
GN ORFNames=BRX43_01915 {ECO:0000313|EMBL:RSU54305.1};
OS Sphingomonas sp. S-NIH.Pt15_0812.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1920129 {ECO:0000313|EMBL:RSU54305.1, ECO:0000313|Proteomes:UP000287772};
RN [1] {ECO:0000313|EMBL:RSU54305.1, ECO:0000313|Proteomes:UP000287772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-NIH.Pt15_0812 {ECO:0000313|EMBL:RSU54305.1,
RC ECO:0000313|Proteomes:UP000287772};
RA Johnson R.C., Deming C., Conlan S., Zellmer C., Michelin A., Lee-Lin S.-Q.,
RA Thomas P.J., Park M., Weingarten R.A., Less J., Dekker J.P., Frank K.M.,
RA Musser K.A., Mcquiston J.R., Henderson D.K., Lau A.F., Palmore T.N.,
RA Segre J.A.;
RT "Genomic and Epidemiologic Investigation to Identify Sphingomonas koreensis
RT Point Sources in an Indolent Hospital Outbreak.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSU54305.1}.
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DR EMBL; QLJH01000002; RSU54305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430BNJ7; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000287772; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:RSU54305.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RSU54305.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287772};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..199
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 380 AA; 40565 MW; 75F3D806E0B34DCB CRC64;
MIDAPGIPLT LIAFVAVIGP LVFIHEMGHY LAGRWFGIKA EAFSIGFGRE VAGWTDRRGT
RWKLGWLPLG GYVKFAGDMN PASQPSAEWL SLPPEERSRT FQAKPVWQRA IVVAAGPLVN
FLAAILILAG FAYLYGVRTA PPVVGAVVQG SPAAAAGLAP GDRILSINGR QMDDFGDLAQ
YAILRPGATV TAMVVRGGGE AAARPLTLRI GETRQSDRFG NQFRIGRLGI ASPPAHYEPV
SLLRAPVEGA SQVVAIVRST IDTLGQIITG RRSVDELGGP LQIAKVSGEQ MSLGWPAFVW
LIAMVSINLG FINLLPVPML DGGHLFFYAI EAVRRRPVGP AAQEWAFRGG LAALLALMVL
VTFNDLGKFG LWRGIAGLIG
//
